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  • 96
    PromoCell normal human dermal fibroblasts
    Normal Human Dermal Fibroblasts, supplied by PromoCell, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC human dermal fibroblasts
    Human Dermal Fibroblasts, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human dermal fibroblasts/product/ATCC
    Average 99 stars, based on 1 article reviews
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    human dermal fibroblasts - by Bioz Stars, 2024-05
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    96
    Lonza certified primary normal human dermal fibroblasts nhdfs
    Threonine 278 and serine 281 of RPS2 are phosphorylated during VacV infection. (A) Western blot analysis of HAP1 cells infected with VacV, HSV-1 or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (B) Western blot analysis of <t>NHDFs</t> infected with VacV, HSV-1, or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (C) Western blot analysis of <t>NHDF</t> lysates that were either mock infected (–) or infected with VacV (+), then treated with recombinant shrimp alkaline phosphatase (rSAP) as indicated. Arrows point to the loss of band-shifted RPS2 in SAP-treated samples. (D,E) NHDFs infected with temperature sensitive (Ts) viral mutants of B1 or F10 kinase for 20 h at permissive (32°C) or non-permissive (39.5°C) temperatures. (F) Structural model of RPS2 with labeled amino acid residues identified as being phosphorylated during VacV infection. (G) MS/MS spectra of RPS2 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (H) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Ex, exogenous RPS2; En, endogenous RPS2. (I) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine substitution mutants (T276A; T278A; S281A) infected with VacV (MOI=5) for 20 h. Exogenous and endogenous forms of RPS2 are indicated. Arrowheads point to unmodified (black) and modified (red) forms of each. (J) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine (T278A; S281A) or glutamic acid (T278E; S281E) substitution mutants infected with VacV (MOI=0.003) for 72 h. (K) Quantification of relative change in viral protein levels presented as mean±s.e.m. (n=4) of NHDFs expressing HA–RPS2 or site-specific alanine mutants (T276A; T278A; S281A) infected with VacV (MOI=0.003) for 72 h. *P<0.05; NS, not statistically significant (unpaired Student's t-test).
    Certified Primary Normal Human Dermal Fibroblasts Nhdfs, supplied by Lonza, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/certified primary normal human dermal fibroblasts nhdfs/product/Lonza
    Average 96 stars, based on 1 article reviews
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    96
    PromoCell fibroblasts
    Threonine 278 and serine 281 of RPS2 are phosphorylated during VacV infection. (A) Western blot analysis of HAP1 cells infected with VacV, HSV-1 or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (B) Western blot analysis of <t>NHDFs</t> infected with VacV, HSV-1, or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (C) Western blot analysis of <t>NHDF</t> lysates that were either mock infected (–) or infected with VacV (+), then treated with recombinant shrimp alkaline phosphatase (rSAP) as indicated. Arrows point to the loss of band-shifted RPS2 in SAP-treated samples. (D,E) NHDFs infected with temperature sensitive (Ts) viral mutants of B1 or F10 kinase for 20 h at permissive (32°C) or non-permissive (39.5°C) temperatures. (F) Structural model of RPS2 with labeled amino acid residues identified as being phosphorylated during VacV infection. (G) MS/MS spectra of RPS2 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (H) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Ex, exogenous RPS2; En, endogenous RPS2. (I) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine substitution mutants (T276A; T278A; S281A) infected with VacV (MOI=5) for 20 h. Exogenous and endogenous forms of RPS2 are indicated. Arrowheads point to unmodified (black) and modified (red) forms of each. (J) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine (T278A; S281A) or glutamic acid (T278E; S281E) substitution mutants infected with VacV (MOI=0.003) for 72 h. (K) Quantification of relative change in viral protein levels presented as mean±s.e.m. (n=4) of NHDFs expressing HA–RPS2 or site-specific alanine mutants (T276A; T278A; S281A) infected with VacV (MOI=0.003) for 72 h. *P<0.05; NS, not statistically significant (unpaired Student's t-test).
    Fibroblasts, supplied by PromoCell, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    PromoCell healthy controls nhdf
    Threonine 278 and serine 281 of RPS2 are phosphorylated during VacV infection. (A) Western blot analysis of HAP1 cells infected with VacV, HSV-1 or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (B) Western blot analysis of <t>NHDFs</t> infected with VacV, HSV-1, or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (C) Western blot analysis of <t>NHDF</t> lysates that were either mock infected (–) or infected with VacV (+), then treated with recombinant shrimp alkaline phosphatase (rSAP) as indicated. Arrows point to the loss of band-shifted RPS2 in SAP-treated samples. (D,E) NHDFs infected with temperature sensitive (Ts) viral mutants of B1 or F10 kinase for 20 h at permissive (32°C) or non-permissive (39.5°C) temperatures. (F) Structural model of RPS2 with labeled amino acid residues identified as being phosphorylated during VacV infection. (G) MS/MS spectra of RPS2 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (H) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Ex, exogenous RPS2; En, endogenous RPS2. (I) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine substitution mutants (T276A; T278A; S281A) infected with VacV (MOI=5) for 20 h. Exogenous and endogenous forms of RPS2 are indicated. Arrowheads point to unmodified (black) and modified (red) forms of each. (J) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine (T278A; S281A) or glutamic acid (T278E; S281E) substitution mutants infected with VacV (MOI=0.003) for 72 h. (K) Quantification of relative change in viral protein levels presented as mean±s.e.m. (n=4) of NHDFs expressing HA–RPS2 or site-specific alanine mutants (T276A; T278A; S281A) infected with VacV (MOI=0.003) for 72 h. *P<0.05; NS, not statistically significant (unpaired Student's t-test).
    Healthy Controls Nhdf, supplied by PromoCell, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Threonine 278 and serine 281 of RPS2 are phosphorylated during VacV infection. (A) Western blot analysis of HAP1 cells infected with VacV, HSV-1 or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (B) Western blot analysis of NHDFs infected with VacV, HSV-1, or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (C) Western blot analysis of NHDF lysates that were either mock infected (–) or infected with VacV (+), then treated with recombinant shrimp alkaline phosphatase (rSAP) as indicated. Arrows point to the loss of band-shifted RPS2 in SAP-treated samples. (D,E) NHDFs infected with temperature sensitive (Ts) viral mutants of B1 or F10 kinase for 20 h at permissive (32°C) or non-permissive (39.5°C) temperatures. (F) Structural model of RPS2 with labeled amino acid residues identified as being phosphorylated during VacV infection. (G) MS/MS spectra of RPS2 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (H) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Ex, exogenous RPS2; En, endogenous RPS2. (I) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine substitution mutants (T276A; T278A; S281A) infected with VacV (MOI=5) for 20 h. Exogenous and endogenous forms of RPS2 are indicated. Arrowheads point to unmodified (black) and modified (red) forms of each. (J) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine (T278A; S281A) or glutamic acid (T278E; S281E) substitution mutants infected with VacV (MOI=0.003) for 72 h. (K) Quantification of relative change in viral protein levels presented as mean±s.e.m. (n=4) of NHDFs expressing HA–RPS2 or site-specific alanine mutants (T276A; T278A; S281A) infected with VacV (MOI=0.003) for 72 h. *P<0.05; NS, not statistically significant (unpaired Student's t-test).

    Journal: Journal of Cell Science

    Article Title: Proteomic and mechanistic dissection of the poxvirus-customized ribosome

    doi: 10.1242/jcs.246603

    Figure Lengend Snippet: Threonine 278 and serine 281 of RPS2 are phosphorylated during VacV infection. (A) Western blot analysis of HAP1 cells infected with VacV, HSV-1 or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (B) Western blot analysis of NHDFs infected with VacV, HSV-1, or VSV (MOI=5) at 20 hpi (for VacV and HSV-1) or 6 hpi (for VSV). Arrowheads point to bandshifted species. (C) Western blot analysis of NHDF lysates that were either mock infected (–) or infected with VacV (+), then treated with recombinant shrimp alkaline phosphatase (rSAP) as indicated. Arrows point to the loss of band-shifted RPS2 in SAP-treated samples. (D,E) NHDFs infected with temperature sensitive (Ts) viral mutants of B1 or F10 kinase for 20 h at permissive (32°C) or non-permissive (39.5°C) temperatures. (F) Structural model of RPS2 with labeled amino acid residues identified as being phosphorylated during VacV infection. (G) MS/MS spectra of RPS2 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (H) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Ex, exogenous RPS2; En, endogenous RPS2. (I) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine substitution mutants (T276A; T278A; S281A) infected with VacV (MOI=5) for 20 h. Exogenous and endogenous forms of RPS2 are indicated. Arrowheads point to unmodified (black) and modified (red) forms of each. (J) Western blot analysis of NHDFs expressing HA–RPS2 or site-specific alanine (T278A; S281A) or glutamic acid (T278E; S281E) substitution mutants infected with VacV (MOI=0.003) for 72 h. (K) Quantification of relative change in viral protein levels presented as mean±s.e.m. (n=4) of NHDFs expressing HA–RPS2 or site-specific alanine mutants (T276A; T278A; S281A) infected with VacV (MOI=0.003) for 72 h. *P<0.05; NS, not statistically significant (unpaired Student's t-test).

    Article Snippet: Certified primary normal human dermal fibroblasts (NHDFs) isolated from human male neonatal foreskin were purchased from Lonza (CC-2509) and grown in Dulbecco's Modified Eagle's Medium (DMEM; Fisher Scientific; MT15013CV) supplemented with 5% FBS, 2 mM L-Glutamine, and penicillin-streptomycin and maintained at 37°C in 5% CO 2 .

    Techniques: Infection, Western Blot, Recombinant, Labeling, Tandem Mass Spectroscopy, Isolation, Sequencing, Expressing, Modification

    RPS28 is expressed at low levels and its modification does not enhance infection in NHDFs. (A) MS/MS spectra of RPS28 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (B) Structural model of RPS28 with labeled amino acid residues identified as being phosphorylated during VacV infection. (C) Western blot analysis of NHDFs expressing HA–RPS28, or site-specific alanine (T38A; S39A) or glutamic acid (T38E; S39E) substitution mutants of HA–RPS28 infected with VacV (MOI=0.003) for 72 h. (D) Western blot analysis of NHDFs expressing HA-RPS28, or double alanine (AA) or glutamic acid (EE) substitution mutants of HA–RPS28 infected with VacV (MOI=0.003) for 72 h. (E) To estimate the relative abundance of RPS2 and RPS28 peptides identified by mass spectroscopy, spectra counts were used as a semi-quantitative measurement and the percentage difference between the total spectra count of identified RPS2 peptides compared to the total spectra count of RPS28 peptides was determined and displayed as the mean±s.e.m. percentage difference relative to the total spectra count of RPS2 (n=5). *P<0.05; NS, not statistically significant (unpaired Student's t-test). (F) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Short and long exposures are shown to illustrate the relative difference in HA–RPS2 versus HA–RPS28 expression.

    Journal: Journal of Cell Science

    Article Title: Proteomic and mechanistic dissection of the poxvirus-customized ribosome

    doi: 10.1242/jcs.246603

    Figure Lengend Snippet: RPS28 is expressed at low levels and its modification does not enhance infection in NHDFs. (A) MS/MS spectra of RPS28 peptides from GFP-TRAP ribosomes isolated from VacV-infected HAP1 cells. The peptide amino acid sequence, phosphorylated residue, b-series ions (blue), y-series ions (red), charge state (+), and ions that support phosphorylation (^) are all indicated. (B) Structural model of RPS28 with labeled amino acid residues identified as being phosphorylated during VacV infection. (C) Western blot analysis of NHDFs expressing HA–RPS28, or site-specific alanine (T38A; S39A) or glutamic acid (T38E; S39E) substitution mutants of HA–RPS28 infected with VacV (MOI=0.003) for 72 h. (D) Western blot analysis of NHDFs expressing HA-RPS28, or double alanine (AA) or glutamic acid (EE) substitution mutants of HA–RPS28 infected with VacV (MOI=0.003) for 72 h. (E) To estimate the relative abundance of RPS2 and RPS28 peptides identified by mass spectroscopy, spectra counts were used as a semi-quantitative measurement and the percentage difference between the total spectra count of identified RPS2 peptides compared to the total spectra count of RPS28 peptides was determined and displayed as the mean±s.e.m. percentage difference relative to the total spectra count of RPS2 (n=5). *P<0.05; NS, not statistically significant (unpaired Student's t-test). (F) Western blot analysis of NHDFs expressing HA–RPS2 or HA–RPS28 protein. Short and long exposures are shown to illustrate the relative difference in HA–RPS2 versus HA–RPS28 expression.

    Article Snippet: Certified primary normal human dermal fibroblasts (NHDFs) isolated from human male neonatal foreskin were purchased from Lonza (CC-2509) and grown in Dulbecco's Modified Eagle's Medium (DMEM; Fisher Scientific; MT15013CV) supplemented with 5% FBS, 2 mM L-Glutamine, and penicillin-streptomycin and maintained at 37°C in 5% CO 2 .

    Techniques: Modification, Infection, Tandem Mass Spectroscopy, Isolation, Sequencing, Labeling, Western Blot, Expressing, Mass Spectrometry